3A.Describe the difference in biological func on of myoglobin and hemoglobin in the body. How does hemoglobin’s sigmoidal O2 binding curve contribute to its biological func on?( Think binding affinity) 3B. Describe the different ways in which the affinity of oxygen to hemoglobin can be modified in vivo

3A.Describe the difference in biological func on of myoglobin and hemoglobin in the body. How does hemoglobin’s sigmoidal O2 binding curve contribute to its biological func on?( Think binding affinity) 3B. Describe the different ways in which the affinity of oxygen to hemoglobin can be modified in vivo

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter11: The Blood

Section: Chapter Questions

Problem 1SQE

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3. When muscles are more active physiological conditions change to affect oxygen binding to Hemoglobin. Briefly describe the changes that occur and why this affects hemoglobin function. Draw the shifted curve on the graph above. A. What physiological conditions change during exercise (levels of what molecules are increasing/decreasing)? B. How do these molecules directly affect Hb’s structure ? What interactions does this stabilize ? C. How do these interactions affect the affinity of Hb for O2? How would this affect the binding curve for Hb? Draw on the graph provided. D. How will this shift in the binding curve affect the function of Hemoglobin ? E.Where does the physiological pO2 in the tissues fall on the O2 binding curve ? In the lungs ? Why is this physiologically important?
A The following plots show an oxygen binding curve for hemoglobin under a certain set of conditions. For each plot, sketch (with reasonable accuracy) a second curve showing how the binding oxygen to hemoglobin would be altered by the change in conditions noted. 2. a. Increase in pCO2 b. Dissociation of native Hb into aß dimers 1 0.8 0.8 0.6 Y 0.4 0.6 Y 0.4 0.2 0.2 poz pO2
2. j The following plots show an oxygen binding curve for hemoglobin under a certain set of conditions. For each plot, sketch (with reasonable accuracy) a second curve showing how the binding of oxygen to hemoglobin would be altered by the change in conditions noted. a. Increase in pCO2 b. Dissociation of native Hb into aß dimers 1 0.8 0.8 0.6 Y 0.4 0.6 Y 0.4 0.2 0.2 po2 pO2
Recall from your BI110 class that metabolically active tissues produce CO2 as a by-product of cellular respiration. Those metabolically active tissues require the O2 that is brought by hemoglobin for the same process (cellular respiration). Explain why the effect of pH on hemoglobin’s affinity for oxygen is consistent with delivering it to actively metabolizing tissues. (Hint: think about what effect the presence of CO2 has on the tissues…)
30. The cooperative binding behavior of hemoglobin for oxygen is best explained by... Group of answer choices The movement of the proximal histidine upon O2 binding causes a structural change at the binding interface between subunits The oxidation of Fe2+ to Fe3+ and formation of the superoxide ion causes distortion of the protoporphyrin ring, altering binding interface between subunits The tetrameric nature of hemoglobin's quaternary structure directly confers cooperative binding activity The movement of the distal histidine upon O2 binding causes a structural change at the binding interface between subunits The binding of O2 causes a pH shift that changes the protonation state of amino acids located at the interface between subunits The solubility of hemoglobin in aqueous solution and its insolubility in nonpolar environments
1. Is this statement correct or incorrect? Explain. During strenuous exercise, the oxygen-hemoglobin dissociation curve shifts to the right. This rightward shift reflects an increase in the affinity of hemoglobin for oxygen and favors loading of O2 onto hemoglobin in the lungs. 2. Is this statement correct or incorrect? Explain. Compared to hemoglobin, myoglobin has a lower binding affinity for O2 and a higher O2 binding capacity, two characteristics that allow myoglobin to efficiently provide skeletal muscle cells with a readily-accessible reservoir of O2.
2.HbF is the predominant hemoglobin of embrions.It has two γ-and two α-subunits(α2γ2).HbF does not bind 2,3-BPG well.What is the affinity of oxygen binding for HbF in compare with HbA?For answer: 1）Explain the function of HbA and the role of 2,3-BPG in the regulation of O2 binding. 2）Draw the oxygen-binding curves of HbA and HbF. 3）Mark the Biology significance of the difference in O2 affinity for HbA and HbF.
3. The image below depicts 2,3-bisphosphoglycerate depicted in dark gray, and ß subunits are depicted in light gray. (BPG) bound to hemoglobin. The a subunits are BPG (a) Briefly explain how BPG regulates oxygen transport by hemoglobin and describe the critical chemical properties of BPG and its binding pocket.
. Oxygen binding by the hemocyanin of the shrimp Callianassa has been measured. Using the following data, prepare a Hill plot and determine (a) Pso, (b) h (the Hill coefficient), and (c) the minimum number of oxygen binding sites on the protein molecule. Poz (mm Hg) Yoz Po, (mm Hg) Yo2 1.1 0.003 136.7 0.557 7.7 0.019 166.8 0.673 10.7 0.035 203.2 0.734 31.7 0.084 262.2 0.794 71.9 0.190 327.0 0.834 100.5 0.329 452.0 0.875 123.3 0.487 736.7 0.913
Hemoglobin and myoglobin both use heme as their prosthetic group and they both bind O2. However, their O2-binding curves indicate these proteins have different activities. What lind of information can be learned about the differences between the curves?
Oxygen affinity of fetal blood is higher than that of maternal blood and may help to provide the fetus with an adequate oxygen supply during pregnancy. In mammals, 2, 3-biphosphosphoglycerate (BPG) mediates intracellular hemoglobin function by lowering cxygen affinity. Fetal red blood cells have higher affinity for oxygen because of a smaller effect of BPG on oxygen affinity of fetal hemoglobin (Hb F) compared with adult Hb (Hb A). Which symbol shows the PS0 value corresponding to Hb F? 14 12 10 0.0 0.5 1.0 1.5 2.0 2,3-BPG (mM) O Crcle O Dimond O Square O Triangle (6H ww) d
Below is the O₂ binding curve for adult Hb in whole blood (containing BPG) shown in red (labelled Hb). Fraction of Hb bound with Oxygen 1.0 0.8 0.6 0.4 0.2 0.0 0 20 40 pO2 (torr) 60 80 ABC c. Which curve lacks cooperativity? [Select] Hb 100 a. Which curve is the best representation for stripped Hb (pure hemoglobin with heme, but no other small allosteric molecules associated)? [Select] b. Which curve has the lowest affinity (as measured by the p50)? [Select]